What does an SH2 domain do?

Src homology 2 (SH2) domains are protein modules (of approximately 100 amino acids) found in many proteins involved in tyrosine kinase signalling cascades. Their function is to bind tyrosine-phosphorylated sequences in specific protein targets.

What proteins have an SH2 domain?

Human proteins containing this domain include:

  • ABL1; ABL2.
  • DAPP1.
  • GRAP; GRAP2; GRB10; GRB14; GRB2; GRB7.
  • HCK; HSH2D.

Does RTKs have SH2 domains?

Once cross-phosphorylated, the cytoplasmic tails of RTKs serve as docking platforms for various intracellular proteins involved in signal transduction. These proteins have a particular domain — called SH2 — that binds to phosphorylated tyrosines in the cytoplasmic RTK receptor tails.

Where is SH2 found?

In cytoplasmic tyrosine kinases, the SH2 domain is located N-terminally to the catalytic kinase domain (SH1) where it mediates cellular localization, substrate recruitment, and regulation of kinase activity.

Is the SH2 domain hydrophobic?

The results suggest that the SH2-domain-mediated activation of Csk is dependent on the binding of the beta3-alphaC loop Ala228 to the hydrophobic pocket formed by the side chains of Tyr116, Tyr133, Leu138, and Leu149 on the surface of the SH2 domain. Copyright (c) 2010 Elsevier Ltd.

What does PTB bind to?

Phosphotyrosine binding (PTB) domains have been identified in a large number of proteins. In proteins like Shc and IRS-1, the PTB domain binds in a phosphotyrosine-dependent fashion to peptides that form a b turn. In these proteins, PTB domains play an important role in signal transduction by growth factor receptors.

What type of protein is SOS?

Essential for normal eye development in Drosophila, SOS has two human homologues, SOS1 and SOS2. The SOS1 gene encodes the Son of Sevenless 1 protein, a Ras and Rac guanine nucleotide exchange factor. This protein is composed of several important domains.

What is Src homology domain?

The Src homology (SH) domains are protein modules with defined structures and protein–protein interaction function that are found in Src family kinases and also in many other intracellular signal transduction proteins, including, for example, receptor protein tyrosine kinases, phospholipase C-gamma, and the Ras GTPase- …

What is SH1 domain?

The SH1 domain is the catalytic domain. The crystal structure of the Src-family tyrosine kinase hck has been solved [7]. Its catalytic (SH1) domain has an overall bilobal structure, with a small ATP-binding N-terminal lobe and a large peptide-binding C-terminal lobe.

How is tyrosine phosphorylated?

Tyrosine phosphorylation is the addition of a phosphate (PO43−) group to the amino acid tyrosine on a protein. This transfer is made possible through enzymes called tyrosine kinases. Tyrosine phosphorylation is a key step in signal transduction and the regulation of enzymatic activity.

What do SOS proteins do?

Mechanistically, the Sos proteins function as enzymatic factors interacting with Ras proteins in response to upstream stimuli to promote guanine nucleotide exchange (GDP/GTP) and subsequent formation of the active Ras-GTP complex.

How is Ras protein activated?

RAS is activated by GDP/GTP exchange stimulated by GEFs and inactivated by GTP hydrolysis stimulated by GAPs. The very slow off-rate for GDP (t1/2 = 6 min, koff = 2 × 10−3 s−1 at 20°) (Hunter et al., 2015) allows RAS proteins to remain in their inactive states until signals provoke GDP/GTP exchange.

Where are the SH2 domains located in a protein?

SH2 domain. The SH2 ( S rc H omology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins.

How does tyrosine phosphorylation affect the SH2 domain?

Tyrosine phosphorylation leads to activation of a cascade of protein-protein interactions whereby SH2 domain-containing proteins are recruited to tyrosine-phosphorylated sites. This process initiates a series of events which eventually result in altered patterns of gene expression or other cellular responses.

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